dbPTM

SFC3_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SFC3_SCHPO
UniProt AC	Q9UST7
Protein Name	Transcription factor tau subunit sfc3
Gene Name	sfc3 {ECO:0000312\|EMBL:CAB58159.1}
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	1339
Subcellular Localization	Nucleus envelope .
Protein Description	TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with sfc6 in DNA binding. Localizes to chromatin insulator sequence without recruiting RNA polymerase III and plays a role in nuclear organization..
Protein Sequence	MDSLIRHCSEEIALDGSSGCSIDRLWEFAANFFFRQGIVQNLDDNYKTFVWPLILKEDGIEVWIEDEDATGLRSKMQEIPWNYQDITIELRARIRLFASEDRQWLTLTYKTKTDSKIQPLAFELLSCISRYRQEGVDRIQLCKETKQEPRSVYGRIQALEDASLISKVAINRSRAQTALLVLKRFESENSTINETVAQVSGKQIYNTEKIRSNICDAVQSSRNGICRHVDARAMVNLNHSRWERRYYARQVTYLHNNGYLRKCLTFVPNSPERCIRCLQFIKPYISSLDATEDDVDFTEVDDIPEDDELEEEEPLLPSKEEFDASFLQPLADVGPTLPQWSRFRPLEFQCFVLIRNAGFHGVITLQILSGLTGIRFNKPLFKLLGSLVEHRSSVPNHLSHMSITRFEDKTKKSRQYRYFTLQSQLNRLIRDGIPAETISKLLPHVHSLAGEFSPIDSSLFLNSLHHKGNMESNAEVSPDGMTLLPRKRGRPRKSANISVTSSPIRPSKNENNLPSLAISPVSEGFIQNATISTPSTSSNLSIAGSLTPSKTSRIYRGLAPLKNPEFNEDHVKKAEHLEPLLNVSSSVPSKNFTVSSPDHLKYGNTSSLQVSDSQSSIDLDSSFHYPVSVDSQLSHSTGSLMANFSSPTKKRRLESVDFIFLQRKGLILSYLVEQNGAFEISRKMFEDLADLKVRRNPETSRTVMDRRTFQQTLEKLMQEKKVRKLVIATNNGLGKLVRKDIVVQYDMKPDSPRFQQLRAQITTPEIEKQSTPEILKDVDVDFLKRNTSLSRRKSMPAEIKRHKESSETKPVDKEEVKKNEKEKDDPMRLAQQLLESLAPDFALHENTQQKSPVEKPKKLRKDRYASVEEFDYFSSTEHASKRSVKRFKNDFTSDEDETLIRAVVITQIYYGGTNRLIKWEAVQKCFPNRDIYALTRRYLSIRQHTKFKGLQQFLSENWQQMYKDAVSRKDLMPYPDSVDDFDPTPYVKASCRPYMISSSNLATTRLPRDLVDVYETYNIEVVKQETNFREMIFDPSLSVASKMNAYCDMPFTMPLSLNDKQNNEGDENCEKGQLFDAKSTIKSIVAIPDATYDARFSQERLMQYPEDILIAAHQELLDKRIITRVNSENSRLQPGRNFQFTEKFASSLKSPLPPFLLSQAKRFNKFLLEGFQNHKNHLFEETSNSGTLACILDLLSQGKLQISIVGSKFNEYGLSEGYRTRLLEHDNINVTLVLSGKESESKKNYGVTEKLATPPSHEPRLWLNGKCELIEMIWMNIEQSIVYQLLRKPGILRSQLTNLLFPGLEPREFNEVLDYFIAAGAAIEKDGLYLNHNYLFKLT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
494	Phosphorylation	KRGRPRKSANISVTS CCCCCCCCCCEEECC	28.03	21712547
498	Phosphorylation	PRKSANISVTSSPIR CCCCCCEEECCCCCC	21.10	24763107
500	Phosphorylation	KSANISVTSSPIRPS CCCCEEECCCCCCCC	19.39	24763107
501	Phosphorylation	SANISVTSSPIRPSK CCCEEECCCCCCCCC	31.77	21712547
502	Phosphorylation	ANISVTSSPIRPSKN CCEEECCCCCCCCCC	18.25	21712547
507	Phosphorylation	TSSPIRPSKNENNLP CCCCCCCCCCCCCCC	37.96	21712547
593	Phosphorylation	SVPSKNFTVSSPDHL CCCCCCEEECCCCCC	28.95	29996109
595	Phosphorylation	PSKNFTVSSPDHLKY CCCCEEECCCCCCCC	32.85	28889911
596	Phosphorylation	SKNFTVSSPDHLKYG CCCEEECCCCCCCCC	29.97	28889911

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of SFC3_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SFC3_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SFC3_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SFC6_SCHPO	sfc6	physical	10906331
SFC1_SCHPO	sfc1	physical	10906331
SFC4_SCHPO	sfc4	physical	10906331
YIQ4_SCHPO	SPAC824.04	genetic	24945319

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SFC3_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595 AND SER-596, ANDMASS SPECTROMETRY.	18257517 [Abstract]